1ifr
From Proteopedia
| Line 1: | Line 1: | ||
| - | [[Image:1ifr.jpg|left|200px]] | + | [[Image:1ifr.jpg|left|200px]] |
| - | + | ||
| - | '''Structure of Lamin A/C Globular Domain''' | + | {{Structure |
| + | |PDB= 1ifr |SIZE=350|CAPTION= <scene name='initialview01'>1ifr</scene>, resolution 1.4Å | ||
| + | |SITE= | ||
| + | |LIGAND= <scene name='pdbligand=GOL:GLYCEROL'>GOL</scene> | ||
| + | |ACTIVITY= | ||
| + | |GENE= | ||
| + | }} | ||
| + | |||
| + | '''Structure of Lamin A/C Globular Domain''' | ||
| + | |||
==Overview== | ==Overview== | ||
| Line 7: | Line 16: | ||
==About this Structure== | ==About this Structure== | ||
| - | 1IFR is a [ | + | 1IFR is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1IFR OCA]. |
==Reference== | ==Reference== | ||
| - | Structure of the globular tail of nuclear lamin., Dhe-Paganon S, Werner ED, Chi YI, Shoelson SE, J Biol Chem. 2002 May 17;277(20):17381-4. Epub 2002 Mar 18. PMID:[http:// | + | Structure of the globular tail of nuclear lamin., Dhe-Paganon S, Werner ED, Chi YI, Shoelson SE, J Biol Chem. 2002 May 17;277(20):17381-4. Epub 2002 Mar 18. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/11901143 11901143] |
[[Category: Homo sapiens]] | [[Category: Homo sapiens]] | ||
[[Category: Single protein]] | [[Category: Single protein]] | ||
| Line 19: | Line 28: | ||
[[Category: immunoglobulin]] | [[Category: immunoglobulin]] | ||
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Mar 20 11:49:51 2008'' |
Revision as of 09:49, 20 March 2008
| |||||||
| , resolution 1.4Å | |||||||
|---|---|---|---|---|---|---|---|
| Ligands: | |||||||
| Coordinates: | save as pdb, mmCIF, xml | ||||||
Structure of Lamin A/C Globular Domain
Overview
The nuclear lamins form a two-dimensional matrix that provides integrity to the cell nucleus and participates in nuclear activities. Mutations in the region of human LMNA encoding the carboxyl-terminal tail Lamin A/C are associated with forms of muscular dystrophy and familial partial lipodystrophy (FPLD). To help discriminate tissue-specific phenotypes, we have solved at 1.4-A resolution the three-dimensional crystal structure of the lamin A/C globular tail. The domain adopts a novel, all beta immunoglobulin-like fold. FPLD-associated mutations cluster within a small surface, whereas muscular dystrophy-associated mutations are distributed throughout the protein core and on its surface. These findings distinguish myopathy- and lipodystrophy-associated mutations and provide a structural framework for further testing hypotheses concerning lamin function.
About this Structure
1IFR is a Single protein structure of sequence from Homo sapiens. Full crystallographic information is available from OCA.
Reference
Structure of the globular tail of nuclear lamin., Dhe-Paganon S, Werner ED, Chi YI, Shoelson SE, J Biol Chem. 2002 May 17;277(20):17381-4. Epub 2002 Mar 18. PMID:11901143
Page seeded by OCA on Thu Mar 20 11:49:51 2008
